NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488154076|ref|WP_002225284|]
View 

sulfate ABC transporter substrate-binding protein [Neisseria meningitidis]

Protein Classification

sulfate ABC transporter substrate-binding protein( domain architecture ID 10004067)

sulfate ABC transporter substrate-binding protein serves as the initial receptor in the ABC transport of sulfate and thiosulfate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Sbp COG1613
ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and ...
 1-350 0e+00

ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and metabolism];


:

Pssm-ID: 441221  Cd Length: 340  Bit Score: 537.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   1 MKTYAPALYTAALLTACSpAADSNHPSGQNApantesdgKNITLLNASYDVARDFYKEYNPLFIKTYQSEHpGTSVSIQQ 80
Cdd:COG1613    1 MKRSQSSLLLAALLALAL-AACAASSAAAAA--------ADVTLLNVSYDPTRELYKEINPAFAKHWKAKT-GQTVTIKQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  81 SHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVEKGWQQALPDHAAPYTSTMVFLVRKNNPKQIRDWNDLAKDGV 160
Cdd:COG1613   71 SHGGSGKQARAVIDGLEADVVTLALAYDIDAIAKAGLIPPDWQKRLPNNSSPYTSTIVFLVRKGNPKGIKDWDDLVKPGV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 161 NIVIANPKTSGNGRYAFLGAYGYGLKTTNGNEQEAQKLVASILKNTPVFENGGRAATTTFTQRNIGDVLITFENEANYVS 240
Cdd:COG1613  151 SVITPNPKTSGGARWNYLAAWGYALKKYGGDEAKAKEFVTKLYKNVPVLDSGARGATTTFVQRGIGDVLLAWENEALLAL 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 241 KKLTQGQFEIVYPSYTISAESPVAVVNSVVAKKGTQKTARAYLEYLWSEPAQELAASLYLRPRNPEVLARHKADFPDLDT 320
Cdd:COG1613  231 KEFGKDKFEIVVPSVSILAEPPVAVVDKNVDKKGTREVAEAYLEYLYSPEAQEIAAKHGYRPRDPEVAAKYAAQFPKLKL 310

                        330       340       350
                 ....*....|....*....|....*....|
gi 488154076 321 FSPEKKFGGWDNIMKTYFADGGIFDRLTAQ 350
Cdd:COG1613  311 FTIDDVFGGWDKAQKTHFADGGIFDQIYAP 340
 
Name Accession Description Interval E-value
Sbp COG1613
ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and ...
 1-350 0e+00

ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441221  Cd Length: 340  Bit Score: 537.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   1 MKTYAPALYTAALLTACSpAADSNHPSGQNApantesdgKNITLLNASYDVARDFYKEYNPLFIKTYQSEHpGTSVSIQQ 80
Cdd:COG1613    1 MKRSQSSLLLAALLALAL-AACAASSAAAAA--------ADVTLLNVSYDPTRELYKEINPAFAKHWKAKT-GQTVTIKQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  81 SHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVEKGWQQALPDHAAPYTSTMVFLVRKNNPKQIRDWNDLAKDGV 160
Cdd:COG1613   71 SHGGSGKQARAVIDGLEADVVTLALAYDIDAIAKAGLIPPDWQKRLPNNSSPYTSTIVFLVRKGNPKGIKDWDDLVKPGV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 161 NIVIANPKTSGNGRYAFLGAYGYGLKTTNGNEQEAQKLVASILKNTPVFENGGRAATTTFTQRNIGDVLITFENEANYVS 240
Cdd:COG1613  151 SVITPNPKTSGGARWNYLAAWGYALKKYGGDEAKAKEFVTKLYKNVPVLDSGARGATTTFVQRGIGDVLLAWENEALLAL 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 241 KKLTQGQFEIVYPSYTISAESPVAVVNSVVAKKGTQKTARAYLEYLWSEPAQELAASLYLRPRNPEVLARHKADFPDLDT 320
Cdd:COG1613  231 KEFGKDKFEIVVPSVSILAEPPVAVVDKNVDKKGTREVAEAYLEYLYSPEAQEIAAKHGYRPRDPEVAAKYAAQFPKLKL 310

                        330       340       350
                 ....*....|....*....|....*....|
gi 488154076 321 FSPEKKFGGWDNIMKTYFADGGIFDRLTAQ 350
Cdd:COG1613  311 FTIDDVFGGWDKAQKTHFADGGIFDQIYAP 340
PBP2_CysP cd01005
Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic ...
 40-348 8.37e-176

Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic binding fold superfamily; This family contains sulfate binding domain of CysP proteins that serve as initial receptors in the ABC transport of sulfate and thiosulfate in eubacteria. After binding the ligand, CysP interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The CysP proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270226  Cd Length: 307  Bit Score: 489.90  E-value: 8.37e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  40 KNITLLNASYDVARDFYKEYNPLFIKTYQSEHpGTSVSIQQSHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVE 119
Cdd:cd01005    1 ADVTLLNVSYDVTRELYEEVNPAFAKYWKEKT-GQTVTIKQSHGGSGKQARAVIDGLEADVVTLALEYDIDRIVKAGLIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 120 KGWQQALPDHAAPYTSTMVFLVRKNNPKQIRDWNDLAKDGVNIVIANPKTSGNGRYAFLGAYGYGLKTtNGNEQEAQKLV 199
Cdd:cd01005   80 PDWQQRLPNNSIPYTSTIVFLVRKGNPKGIRDWDDLVKPGVSVITPNPKTSGGARWNYLAAWGYALKK-GGSEAKAKEFV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 200 ASILKNTPVFENGGRAATTTFTQRNIGDVLITFENEANYVSKKLTQGQFEIVYPSYTISAESPVAVVNSVVAKKGTQKTA 279
Cdd:cd01005  159 TSLYKNVPVLDSGAREATTTFVKRGIGDVLITWENEAILANKELGGDKFEIVYPSVSILAEPPVAVVDKNVDKHGTREVA 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488154076 280 RAYLEYLWSEPAQELAASLYLRPRNPEVLARHKADFPDLDTFSPEKKFGGWDNIMKTYFADGGIFDRLT 348
Cdd:cd01005  239 EAYLEFLYSPEAQEIAAKNGYRPRDPEVAAKYAKQFPAINLFFIIDDFGGWAKAQKKHFGDGGIFDQIY 307
3a0106s03 TIGR00971
sulfate/thiosulfate-binding protein; This model describes binding proteins functionally ...
 40-347 4.41e-131

sulfate/thiosulfate-binding protein; This model describes binding proteins functionally associated with the sulfate ABC transporter. In the model bacterium E. coli, two different members work with the same transporter; mutation analysis says each enables the uptake of both sulfate and thiosulfate. In many species, a single binding protein is found, and may be referred to in general terms as a sulfate ABC transporter sulfate-binding protein. [Transport and binding proteins, Anions]


Pssm-ID: 130044  Cd Length: 315  Bit Score: 377.00  E-value: 4.41e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   40 KNITLLNASYDVARDFYKEYNPLFIKTYQSEHpGTSVSIQQSHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVE 119
Cdd:TIGR00971   9 KDIQLLNVSYDPTRELYEQYNKAFEAHWKQET-GDNVVIRQSHGGSGKQATSVINGIEADVVTLALAYDVDAIAERGRID 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  120 KGWQQALPDHAAPYTSTMVFLVRKNNPKQIRDWNDLAKDGVNIVIANPKTSGNGRYAFLGAYGYGLKTTNGNEQEAQKLV 199
Cdd:TIGR00971  88 KDWIKRLPDNSAPYTSTIVFLVRKGNPKQIHDWNDLIKPGVSVITPNPKSSGGARWNYLAAWGYALHHNNGDQAKAQQFV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  200 ASILKNTPVFENGGRAATTTFTQRNIGDVLITFENEANYVSKKLTQGQFEIVYPSYTISAESPVAVVNSVVAKKGTQKTA 279
Cdd:TIGR00971 168 TALLKNVEVLDSGARGATNTFVERGIGDVLIAWENEALLARKELGKDKFEIVTPSESILAEPTVSVVDKVVEKKGTKKVA 247

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488154076  280 RAYLEYLWSEPAQELAASLYLRPRNPEVLARHKADFPDLDTFSPEKKFGGWDNIMKTYFADGGIFDRL 347
Cdd:TIGR00971 248 EAYLKYLYSPEGQEIAAKNYYRPRDAEVAKKYEDKFPKLKLFTIDDKFGGWPKAQKTHFANGGTFDQI 315
PRK10752 PRK10752
sulfate ABC transporter substrate-binding protein;
40-347 1.26e-125

sulfate ABC transporter substrate-binding protein;


Pssm-ID: 182700  Cd Length: 329  Bit Score: 363.73  E-value: 1.26e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  40 KNITLLNASYDVARDFYKEYNPLFIKTYQSEhPGTSVSIQQSHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVE 119
Cdd:PRK10752  20 KDIQLLNVSYDPTRELYEQYNKAFSAHWKQQ-TGDNVVIRQSHGGSGKQATSVINGIEADVVTLALAYDVDAIAERGRID 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 120 KGWQQALPDHAAPYTSTMVFLVRKNNPKQIRDWNDLAKDGVNIVIANPKTSGNGRYAFLGAYGYGLKTTNGNEQEAQKLV 199
Cdd:PRK10752  99 KNWIKRLPDNSAPYTSTIVFLVRKGNPKQIHDWNDLIKPGVSVITPNPKSSGGARWNYLAAWGYALHHNNNDQAKAQDFV 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 200 ASILKNTPVFENGGRAATTTFTQRNIGDVLITFENEANYVSKKLTQGQFEIVYPSYTISAESPVAVVNSVVAKKGTQKTA 279
Cdd:PRK10752 179 KALYKNVEVLDSGARGSTNTFVERGIGDVLIAWENEALLAANELGKDKFEIVTPSESILAEPTVSVVDKVVDKKGTREVA 258

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488154076 280 RAYLEYLWSEPAQELAASLYLRPRNPEVLARHKADFPDLDTFSPEKKFGGWDNIMKTYFADGGIFDRL 347
Cdd:PRK10752 259 EAYLKYLYSPEGQEIAAKNYYRPRDAEVAKKYENAFPKLKLFTIDEVFGGWTKAQKEHFANGGTFDQI 326
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 74-297 3.64e-35

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 128.15  E-value: 3.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   74 TSVSIQQSHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVEKGWQQALpdhaapYTSTMVFLVRKNNPKQIRDWN 153
Cdd:pfam13531  23 TGVKVVVSYGGSGKLAKQIANGAPADVFISADSAWLDKLAAAGLVVPGSRVPL------AYSPLVIAVPKGNPKDISGLA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  154 DLAKDGVNIVIANPKTSGNGRYA--FLGAYGyglkttngneqeaqkLVASILKNTPVFENGGRAATTTFTQRNiGDVLIT 231
Cdd:pfam13531  97 DLLKPGVRLAVADPKTAPSGRAAleLLEKAG---------------LLKALEKKVVVLGENVRQALTAVASGE-ADAGIV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488154076  232 FENEANYVSKKltqGQFEIVYP--SYTISAESPVAVVNsvvaKKGTQKTARAYLEYLWSEPAQELAAS 297
Cdd:pfam13531 161 YLSEALFPENG---PGLEVVPLpeDLNLPLDYPAAVLK----KAAHPEAARAFLDFLLSPEAQAILRK 221
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
 88-301 3.76e-03

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 38.08  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076    88 QALSVANGLQADVVTMNQSSDIDLLeKKGLVEKGWQQALP--------DHAAPY-TSTMVFLVRKNNPkqIRDWNDLAkd 158
Cdd:smart00062  31 KAIAKELGLKVEFVEVSFDSLLTAL-KSGKIDVVAAGMTItperakqvDFSDPYyRSGQVILVRKDSP--IKSLEDLK-- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   159 gvNIVIANPKTSGNGRYAFLGAYGYGLKTTNGNEQEAQKLVAsilkntpvfengGRAatttftqrnigDVLITFENEANY 238
Cdd:smart00062 106 --GKKVAVVAGTTAEELLKKLYPEAKIVSYDSNAEALAALKA------------GRA-----------DAAVADAPLLAA 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488154076   239 VSKKLTQGQFEIVYPSYTISAESPVAVvnsvvaKKGTQKTARAYLEYLWSEPAQELAASLYLR 301
Cdd:smart00062 161 LVKQHGLPELKIVPDPLDTPEGYAIAV------RKGDPELLDKINKALKELKADGTLKKISEK 217
 
Name Accession Description Interval E-value
Sbp COG1613
ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and ...
 1-350 0e+00

ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441221  Cd Length: 340  Bit Score: 537.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   1 MKTYAPALYTAALLTACSpAADSNHPSGQNApantesdgKNITLLNASYDVARDFYKEYNPLFIKTYQSEHpGTSVSIQQ 80
Cdd:COG1613    1 MKRSQSSLLLAALLALAL-AACAASSAAAAA--------ADVTLLNVSYDPTRELYKEINPAFAKHWKAKT-GQTVTIKQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  81 SHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVEKGWQQALPDHAAPYTSTMVFLVRKNNPKQIRDWNDLAKDGV 160
Cdd:COG1613   71 SHGGSGKQARAVIDGLEADVVTLALAYDIDAIAKAGLIPPDWQKRLPNNSSPYTSTIVFLVRKGNPKGIKDWDDLVKPGV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 161 NIVIANPKTSGNGRYAFLGAYGYGLKTTNGNEQEAQKLVASILKNTPVFENGGRAATTTFTQRNIGDVLITFENEANYVS 240
Cdd:COG1613  151 SVITPNPKTSGGARWNYLAAWGYALKKYGGDEAKAKEFVTKLYKNVPVLDSGARGATTTFVQRGIGDVLLAWENEALLAL 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 241 KKLTQGQFEIVYPSYTISAESPVAVVNSVVAKKGTQKTARAYLEYLWSEPAQELAASLYLRPRNPEVLARHKADFPDLDT 320
Cdd:COG1613  231 KEFGKDKFEIVVPSVSILAEPPVAVVDKNVDKKGTREVAEAYLEYLYSPEAQEIAAKHGYRPRDPEVAAKYAAQFPKLKL 310

                        330       340       350
                 ....*....|....*....|....*....|
gi 488154076 321 FSPEKKFGGWDNIMKTYFADGGIFDRLTAQ 350
Cdd:COG1613  311 FTIDDVFGGWDKAQKTHFADGGIFDQIYAP 340
PBP2_CysP cd01005
Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic ...
 40-348 8.37e-176

Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic binding fold superfamily; This family contains sulfate binding domain of CysP proteins that serve as initial receptors in the ABC transport of sulfate and thiosulfate in eubacteria. After binding the ligand, CysP interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The CysP proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270226  Cd Length: 307  Bit Score: 489.90  E-value: 8.37e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  40 KNITLLNASYDVARDFYKEYNPLFIKTYQSEHpGTSVSIQQSHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVE 119
Cdd:cd01005    1 ADVTLLNVSYDVTRELYEEVNPAFAKYWKEKT-GQTVTIKQSHGGSGKQARAVIDGLEADVVTLALEYDIDRIVKAGLIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 120 KGWQQALPDHAAPYTSTMVFLVRKNNPKQIRDWNDLAKDGVNIVIANPKTSGNGRYAFLGAYGYGLKTtNGNEQEAQKLV 199
Cdd:cd01005   80 PDWQQRLPNNSIPYTSTIVFLVRKGNPKGIRDWDDLVKPGVSVITPNPKTSGGARWNYLAAWGYALKK-GGSEAKAKEFV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 200 ASILKNTPVFENGGRAATTTFTQRNIGDVLITFENEANYVSKKLTQGQFEIVYPSYTISAESPVAVVNSVVAKKGTQKTA 279
Cdd:cd01005  159 TSLYKNVPVLDSGAREATTTFVKRGIGDVLITWENEAILANKELGGDKFEIVYPSVSILAEPPVAVVDKNVDKHGTREVA 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488154076 280 RAYLEYLWSEPAQELAASLYLRPRNPEVLARHKADFPDLDTFSPEKKFGGWDNIMKTYFADGGIFDRLT 348
Cdd:cd01005  239 EAYLEFLYSPEAQEIAAKNGYRPRDPEVAAKYAKQFPAINLFFIIDDFGGWAKAQKKHFGDGGIFDQIY 307
CysP COG4150
ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and ...
 1-351 1.33e-155

ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443321  Cd Length: 334  Bit Score: 439.74  E-value: 1.33e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   1 MKTYAPALYTAALLTACSPAADSnhpsgqnapantesdgkniTLLNASYDVARDFYKEYNPLFIKTYQSEHpGTSVSIQQ 80
Cdd:COG4150    3 MKKLLLAGAAALALAAPAAAAAT-------------------ELLNSSYDIARELFAALNPAFVAQWKAQT-GDDLTIKQ 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  81 SHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKG-LVEKGWQQALPDHAAPYTSTMVFLVRKNNPKQIRDWNDLAKDG 159
Cdd:COG4150   63 SHAGSSKQARAILQGLKADVVTFNQVTDVQILHDKGnLIPADWQARLPNNSSPYYSTMAFLVRKGNPKNIKDWDDLARDD 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 160 VNIVIANPKTSGNGRYAFLGAYGYGLKTTNGNEQEAQKLVASILKNTPVFENGGRAATTTFTQRNIGDVLITFENEANYV 239
Cdd:COG4150  143 VKLVFPNPKTSGNGRYTYLAAWGYALEAFGGDEAKTREFMKKFLANVAVFDTGGRGATTTFVERGIGDVLITFESEVNNI 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 240 SKKLTQGQFEIVYPSYTISAESPVAVVNSVVAKKGTQKTARAYLEYLWSEPAQELAASLYLRPRNPEVLARHKADFPDLD 319
Cdd:COG4150  223 RKQYGADGYEVVVPPVSILAEFPVAVVDKNVEKNGTEEAAKAYLNYLYSPEAQRILAGFNYRVNDEAVAAEFADRFPEVK 302

                        330       340       350
                 ....*....|....*....|....*....|..
gi 488154076 320 TFSPEKKFGGWDNIMKTYFADGGIFDRLTAQK 351
Cdd:COG4150  303 LFTVEDVFGGWDQVMKTHFASGGELDQLLAAG 334
3a0106s03 TIGR00971
sulfate/thiosulfate-binding protein; This model describes binding proteins functionally ...
 40-347 4.41e-131

sulfate/thiosulfate-binding protein; This model describes binding proteins functionally associated with the sulfate ABC transporter. In the model bacterium E. coli, two different members work with the same transporter; mutation analysis says each enables the uptake of both sulfate and thiosulfate. In many species, a single binding protein is found, and may be referred to in general terms as a sulfate ABC transporter sulfate-binding protein. [Transport and binding proteins, Anions]


Pssm-ID: 130044  Cd Length: 315  Bit Score: 377.00  E-value: 4.41e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   40 KNITLLNASYDVARDFYKEYNPLFIKTYQSEHpGTSVSIQQSHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVE 119
Cdd:TIGR00971   9 KDIQLLNVSYDPTRELYEQYNKAFEAHWKQET-GDNVVIRQSHGGSGKQATSVINGIEADVVTLALAYDVDAIAERGRID 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  120 KGWQQALPDHAAPYTSTMVFLVRKNNPKQIRDWNDLAKDGVNIVIANPKTSGNGRYAFLGAYGYGLKTTNGNEQEAQKLV 199
Cdd:TIGR00971  88 KDWIKRLPDNSAPYTSTIVFLVRKGNPKQIHDWNDLIKPGVSVITPNPKSSGGARWNYLAAWGYALHHNNGDQAKAQQFV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  200 ASILKNTPVFENGGRAATTTFTQRNIGDVLITFENEANYVSKKLTQGQFEIVYPSYTISAESPVAVVNSVVAKKGTQKTA 279
Cdd:TIGR00971 168 TALLKNVEVLDSGARGATNTFVERGIGDVLIAWENEALLARKELGKDKFEIVTPSESILAEPTVSVVDKVVEKKGTKKVA 247

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488154076  280 RAYLEYLWSEPAQELAASLYLRPRNPEVLARHKADFPDLDTFSPEKKFGGWDNIMKTYFADGGIFDRL 347
Cdd:TIGR00971 248 EAYLKYLYSPEGQEIAAKNYYRPRDAEVAKKYEDKFPKLKLFTIDDKFGGWPKAQKTHFANGGTFDQI 315
PRK10752 PRK10752
sulfate ABC transporter substrate-binding protein;
40-347 1.26e-125

sulfate ABC transporter substrate-binding protein;


Pssm-ID: 182700  Cd Length: 329  Bit Score: 363.73  E-value: 1.26e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  40 KNITLLNASYDVARDFYKEYNPLFIKTYQSEhPGTSVSIQQSHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVE 119
Cdd:PRK10752  20 KDIQLLNVSYDPTRELYEQYNKAFSAHWKQQ-TGDNVVIRQSHGGSGKQATSVINGIEADVVTLALAYDVDAIAERGRID 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 120 KGWQQALPDHAAPYTSTMVFLVRKNNPKQIRDWNDLAKDGVNIVIANPKTSGNGRYAFLGAYGYGLKTTNGNEQEAQKLV 199
Cdd:PRK10752  99 KNWIKRLPDNSAPYTSTIVFLVRKGNPKQIHDWNDLIKPGVSVITPNPKSSGGARWNYLAAWGYALHHNNNDQAKAQDFV 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 200 ASILKNTPVFENGGRAATTTFTQRNIGDVLITFENEANYVSKKLTQGQFEIVYPSYTISAESPVAVVNSVVAKKGTQKTA 279
Cdd:PRK10752 179 KALYKNVEVLDSGARGSTNTFVERGIGDVLIAWENEALLAANELGKDKFEIVTPSESILAEPTVSVVDKVVDKKGTREVA 258

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488154076 280 RAYLEYLWSEPAQELAASLYLRPRNPEVLARHKADFPDLDTFSPEKKFGGWDNIMKTYFADGGIFDRL 347
Cdd:PRK10752 259 EAYLKYLYSPEGQEIAAKNYYRPRDAEVAKKYENAFPKLKLFTIDEVFGGWTKAQKEHFANGGTFDQI 326
PRK10852 PRK10852
thiosulfate ABC transporter substrate-binding protein CysP;
43-349 1.37e-124

thiosulfate ABC transporter substrate-binding protein CysP;


Pssm-ID: 236775  Cd Length: 338  Bit Score: 361.38  E-value: 1.37e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  43 TLLNASYDVARDFYKEYNPLFIKTYQSEHPGTSVSIQQSHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKG-LVEKG 121
Cdd:PRK10852  27 ELLNSSYDVSRELFAALNPPFEQQWAKDNPGDKLTIKQSHAGSSKQALAILQGLKADVVTYNQVTDVQILHDKGkLIPAD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 122 WQQALPDHAAPYTSTMVFLVRKNNPKQIRDWNDLAKDGVNIVIANPKTSGNGRYAFLGAYGYGLKTTNGNEQEAQKLVAS 201
Cdd:PRK10852 107 WQSRLPNNSSPFYSTMAFLVRKGNPKNIHDWNDLVRSDVKLIFPNPKTSGNARYTYLAAWGAADKADGGDKAKTEQFMTQ 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 202 ILKNTPVFENGGRAATTTFTQRNIGDVLITFENEANYVSKKLTQGQFEIVYPSYTISAESPVAVVNSVVAKKGTQKTARA 281
Cdd:PRK10852 187 FLKNVEVFDTGGRGATTTFAERGLGDVLISFESEVNNIRKQYEAQGYEVVVPKTNILAEFPVAWVDKNVQANGTEKAAKA 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488154076 282 YLEYLWSEPAQELAASLYLRPRNPEVLARHKADFPDLDTFSPEKKFGGWDNIMKTYFADGGIFDRLTA 349
Cdd:PRK10852 267 YLNYLYSPQAQTIITDFYYRVNNPEVMDKLKDKFPQTELFRVEDKFGSWPEVMKTHFTSGGELDKLLA 334
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 74-297 3.64e-35

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 128.15  E-value: 3.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   74 TSVSIQQSHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVEKGWQQALpdhaapYTSTMVFLVRKNNPKQIRDWN 153
Cdd:pfam13531  23 TGVKVVVSYGGSGKLAKQIANGAPADVFISADSAWLDKLAAAGLVVPGSRVPL------AYSPLVIAVPKGNPKDISGLA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  154 DLAKDGVNIVIANPKTSGNGRYA--FLGAYGyglkttngneqeaqkLVASILKNTPVFENGGRAATTTFTQRNiGDVLIT 231
Cdd:pfam13531  97 DLLKPGVRLAVADPKTAPSGRAAleLLEKAG---------------LLKALEKKVVVLGENVRQALTAVASGE-ADAGIV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488154076  232 FENEANYVSKKltqGQFEIVYP--SYTISAESPVAVVNsvvaKKGTQKTARAYLEYLWSEPAQELAAS 297
Cdd:pfam13531 161 YLSEALFPENG---PGLEVVPLpeDLNLPLDYPAAVLK----KAAHPEAARAFLDFLLSPEAQAILRK 221
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
 64-293 6.19e-17

ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440489 [Multi-domain]  Cd Length: 253  Bit Score: 79.14  E-value: 6.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  64 IKTYQSEHPGTSVSIqqSHGGSSKQALSVANGLQADVVTmnqSSD---IDLLEKKGLVEKGWQQALpdhaApyTSTMVFL 140
Cdd:COG0725   43 AAAFEKEHPGVKVEL--SFGGSGALARQIEQGAPADVFI---SADekyMDKLAKKGLILAGSRVVF----A--TNRLVLA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 141 VRKNNPKQIRDWNDLAKDGVNIVIANPKTSGNGRYAflgaygyglkttngneQEA-QKL-VASILKNTPVFENGGRaATT 218
Cdd:COG0725  112 VPKGNPADISSLEDLAKPGVRIAIGDPKTVPYGKYA----------------KEAlEKAgLWDALKPKLVLGENVR-QVL 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488154076 219 TFTQRNIGDVLITFENEANYVSKKLTQGQFEivyPSYTISAESPVAVVNSvvAKKgtQKTARAYLEYLWSEPAQE 293
Cdd:COG0725  175 AYVESGEADAGIVYLSDALAAKGVLVVVELP---AELYAPIVYPAAVLKG--AKN--PEAAKAFLDFLLSPEAQA 242
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 93-323 2.12e-13

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 69.58  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  93 ANGLQADVVTMNQSSDIDLLEKKGLVE----KGWQQaLPDHAAP--------YTSTMVFLVRKNNPKQI---RDWNDLAK 157
Cdd:COG1840   31 GGNPPADVVWSGDADALEQLANEGLLQpyksPELDA-IPAEFRDpdgywfgfSVRARVIVYNTDLLKELgvpKSWEDLLD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 158 D---GvNIVIANPKTSGNGrYAFLGAygygLKTTNGnEQEAQKLVASILKNTPVFENGGRAATTTFTQrniGDVLITFEN 234
Cdd:COG1840  110 PeykG-KIAMADPSSSGTG-YLLVAA----LLQAFG-EEKGWEWLKGLAANGARVTGSSSAVAKAVAS---GEVAIGIVN 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 235 EANYVSKKLTQGQFEIVYPS-YTISAESPVAVVNSvvAKKgtQKTARAYLEYLWSEPAQE-LAASLYLRPRNPEVLArhK 312
Cdd:COG1840  180 SYYALRAKAKGAPVEVVFPEdGTLVNPSGAAILKG--APN--PEAAKLFIDFLLSDEGQElLAEEGYEYPVRPDVEP--P 253

                        250
                 ....*....|.
gi 488154076 313 ADFPDLDTFSP 323
Cdd:COG1840  254 EGLPPLGELKL 264
PBP2_PEB3_AcfC cd13519
Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a ...
 133-294 3.49e-11

Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a member of the type 2 periplasmic binding fold superfamily; PEB3 is a glycoprotein adhesion from Campylobacter jejuni whose structure suggests a functional role in transport, and resembles PEB1a, an Asp/Glu transporter and an adhesin. The overall structure of PEB3 is a dimer and is similar to that of other type 2 periplasmic transport proteins such as the molybdate/tungstate, sulfate, and ferric iron transporters. PEB3 has high sequence identity to Paa, an Escherichia coli adhesin, and to AcfC, an accessory colonization factor from Vibrio cholera.


Pssm-ID: 270237 [Multi-domain]  Cd Length: 227  Bit Score: 62.33  E-value: 3.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 133 YTSTMVFLVRKNNPKQIRDWNDLAKDGVNIVIANpktsgngryaflGAYGYGLKTTNGNEQEAQKLVASILKNTPVFENG 212
Cdd:cd13519   78 YLRPSAILVRKGNPKKIKGLKDLLKPGVKILVVN------------GAGQTGLWEDMAGRTGDIETVRAFRKNIVVFAKN 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 213 GRAATTTFTQRNIGDVLITFENEANYVSkklTQGQFEIVYPSYTISAESPVAvvnsvVAKKGTQ-KTARAYLEYLWSEPA 291
Cdd:cd13519  146 SGAARKAWKQDPNIDAWITWNIWQKANP---DIADFVELEKDYVIYRDMNVA-----LTKKGLQnPEAQEFIDYLSSKEA 217


                 ...
gi 488154076 292 QEL 294
Cdd:cd13519  218 QAI 220
PBP2_ModA_like_1 cd13538
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ...
 65-297 2.17e-10

Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270256 [Multi-domain]  Cd Length: 230  Bit Score: 60.01  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  65 KTYQSEHPGTSVSIqqSHGGSSKQALSVANGLQADV-VTMNQSSdIDLLEKKGLVEkgwqqalpDHAAPYTS-TMVFLVR 142
Cdd:cd13538   19 EQFEKSNPGVKVTF--NFAGSQALVTQIEQGAPADVfASADTAN-MDALVKAGLLV--------DTPTIFATnKLVVIVP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 143 KNNPKQIRDWNDLAKDGVNIVIANPkTSGNGRYA--FLGAygygLKTTNGNEQEAQklvasILKNTPVFENggraatttf 220
Cdd:cd13538   88 KDNPAKITSLADLAKPGVKIVIGAP-EVPVGTYTrrVLDK----AGNDYAYGYKEA-----VLANVVSEET--------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 221 tqrNIGDVL-----------ITFENEANYVSKKLTQgqfeIVYP-SYTISAESPVAVVNSvvAKKgtQKTARAYLEYLWS 288
Cdd:cd13538  149 ---NVRDVVtkvalgeadagFVYVTDAKAASEKLKV----ITIPeEYNVTATYPIAVLKA--SKN--PELARAFVDFLLS 217


                 ....*....
gi 488154076 289 EPAQELAAS 297
Cdd:cd13538  218 EEGQAILAE 226
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 64-302 5.39e-10

Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270265 [Multi-domain]  Cd Length: 259  Bit Score: 59.16  E-value: 5.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  64 IKTYQSEHPGTSVSIQQSHGGS--SK-QALSVANGLQADVVTMNQSSDIDLLEKKGLVEKGWQ-------QALPDHAAPY 133
Cdd:cd13547   17 VEAFEKKYPGVKVEVFRAGTGKlmAKlAAEAEAGNPQADVLWVADPPTAEALKKEGLLLPYKSpeadaipAPFYDKDGYY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 134 T----STMVFLVRKNNPKQIR--DWNDLAKDGVN--IVIANPKTSGNGRY---AFLGAYGY-----------GLKTTNGN 191
Cdd:cd13547   97 YgtrlSAMGIAYNTDKVPEEApkSWADLTKPKYKgqIVMPDPLYSGAALDlvaALADKYGLgweyfeklkenGVKVEGGN 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 192 EQEAQKLvasilkntpvfENGGRAAtttftqrnigdVLITFENEANYVSKKLTqgqFEIVYP-SYTISAESPVAVVnsvv 270
Cdd:cd13547  177 GQVLDAV-----------ASGERPA-----------GVGVDYNALRAKEKGSP---LEVIYPeEGTVVIPSPIAIL---- 227

                        250       260       270
                 ....*....|....*....|....*....|....
gi 488154076 271 akKGT--QKTARAYLEYLWSEPAQELAASLYLRP 302
Cdd:cd13547  228 --KGSknPEAAKAFVDFLLSPEGQELVADAGLLP 259
PBP2_ModA3_like cd13517
Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 ...
 82-176 2.07e-08

Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 periplasmic binding fold superfamily; This subfamily contains molybdate binding protein-like (ModA3) domain of an ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. ModA transporters import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arrangted around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270235 [Multi-domain]  Cd Length: 223  Bit Score: 54.15  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  82 HGGSSKQALS-VANGLQADVVTMNQSSDIDLLEKKGLVE--KGWQQALPdhaapytstmVFLVRKNNPKQIRDWNDLAKD 158
Cdd:cd13517   32 TYGGSGQLLSqIETSKKGDVFIPGSEDYMEKAKEKGLVEtvKIVAYHVP----------VIAVPKGNPKNITSLEDLAKP 101

                         90
                 ....*....|....*...
gi 488154076 159 GVNIVIANPKTSGNGRYA 176
Cdd:cd13517  102 GVKVALGDPKAAAIGKYA 119
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 97-302 2.63e-08

Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The iron- and thiamine-binding proteins belong to the PBPI2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270236 [Multi-domain]  Cd Length: 260  Bit Score: 54.23  E-value: 2.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  97 QADVVTMNQSSDIDLLEKKGLVEK-GWQQALPDHAAP------YTSTM----VFLVRKNNPKQI---RDWNDLAKDGVN- 161
Cdd:cd13518   50 QADVFWGGEIIALEALKEEGLLEPyTPKVIEAIPADYrdpdgyWVGFAararVFIYNTDKLKEPdlpKSWDDLLDPKWKg 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 162 -IVIANPKTSGNGrYAFLGAygygLKTTNGNEQEAQKLVASILKNTPVFENGGRAATTTFTQRNigDVLITFENEA-NYV 239
Cdd:cd13518  130 kIVYPTPLRSGTG-LTHVAA----LLQLMGEEKGGWYLLKLLANNGKPVAGNSDAYDLVAKGEV--AVGLTDTYYAaRAA 202

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488154076 240 SKKLTqgqFEIVYPsytisAESPVAVVNSVVAKKGTQK--TARAYLEYLWSEPAQE-LAASLYLRP 302
Cdd:cd13518  203 AKGEP---VEIVYP-----DQGALVIPEGVALLKGAPNpeAAKKFIDFLLSPEGQKaLAAANAQLP 260
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 133-336 4.33e-07

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 50.44  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  133 YTSTMVFLVRK---NNPKQIRDWNDLA----KDGVNIVIANPKTSGNgryAFLGAygygLKTTNGnEQEAQKLVASILKN 205
Cdd:pfam13343  60 GVGPLVIAYNKerlGGRPVPRSWADLLdpeyKGKVALPGPNVGDLFN---ALLLA----LYKDFG-EDGVRKLARNLKAN 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  206 TPVFENGGRAATTTFTQRNIGdVLITFENEAnYVSKKltqGQFEIVYPsytisAESPVAVVNSVVAKKGTQKTARAYLEY 285
Cdd:pfam13343 132 LHPAQMVKAAGRLESGEPAVY-LMPYFFADI-LPRKK---KNVEVVWP-----EDGALVSPIFMLVKKGKKELADPLIDF 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488154076  286 LWSEPAQE-LAASLYLRP--RNPEVlarhKADFPDLDTFspekKFGGWDNIMKT 336
Cdd:pfam13343 202 LLSPEVQAiLAKAGLVFPvvLNPAV----DNPLPEGAPF----KWLGWDYIRKN 247
PBP2_YvgL_like cd13537
Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the ...
 64-176 8.07e-07

Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. ModA proteins serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate and tungstate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270255 [Multi-domain]  Cd Length: 225  Bit Score: 49.21  E-value: 8.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  64 IKTYQSEHPGtsVSIQQSHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVEKGWQQALPDHaapytsTMVFLVRK 143
Cdd:cd13537   18 ATEYEKENPG--VKITFNFGGSGTLQKQIESGAPADVFFSAAKKQMDALEDKGLIDASTRKNLLKN------KLVLIVPK 89

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488154076 144 NNPKQIRDWNDLAKDGVNIVIANPKTSGNGRYA 176
Cdd:cd13537   90 DSDSKISSFDLTKDDVKKIAIGEPETVPAGKYA 122
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 63-293 1.34e-06

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 49.34  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   63 FIKTYQSEHPGTSVSIQQSHGGSSKQALSV---ANGLQADVVTMNqSSDIDLLEKKGLVE--------KGWQQALPDHAA 131
Cdd:pfam01547  13 LVKEFEKEHPGIKVEVESVGSGSLAQKLTTaiaAGDGPADVFASD-NDWIAELAKAGLLLplddyvanYLVLGVPKLYGV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  132 PYTS-TMVFLVRKNNPKQ-----IRDWNDLAKDGVNIVIANPKTSGNGRYAFLG---------AYGYGLKTTNGNEQE-- 194
Cdd:pfam01547  92 PLAAeTLGLIYNKDLFKKagldpPKTWDELLEAAKKLKEKGKSPGGAGGGDASGtlgyftlalLASLGGPLFDKDGGGld 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  195 ---------------AQKLVASILKNTPVFENGGRAATTTFTQRNIgDVLITFENEANYVSKKLTQGQFEIVYPSY---- 255
Cdd:pfam01547 172 npeavdaityyvdlyAKVLLLKKLKNPGVAGADGREALALFEQGKA-AMGIVGPWAALAANKVKLKVAFAAPAPDPkgdv 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 488154076  256 ------TISAESPVAVVNSVVAKKGTQKTARAYLEYLWSEPAQE 293
Cdd:pfam01547 251 gyaplpAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
 152-307 6.73e-06

Substrate binding domain of a putative ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270262 [Multi-domain]  Cd Length: 292  Bit Score: 47.21  E-value: 6.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 152 WNDLAKDGV--NIVIANPKTSGNGrYAFLgaygYGLKTTNGnEQEAQKLVASILKNTPVFENGG-----RAATTTFTqrn 224
Cdd:cd13544  121 WEDLLNPEYkgEIVMPNPASSGTA-YTFL----ASLIQLMG-EDEAWEYLKKLNKNVGQYTKSGsapakLVASGEAA--- 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 225 IGdvlITFENEAnyVSKKLTQGQFEIVYPSYTISAE-SPVAVVnsvvakKGT--QKTARAYLEYLWSEPAQELAA--SLY 299
Cdd:cd13544  192 IG---ISFLHDA--LKLKEQGYPIKIIFPKEGTGYEiEAVAII------KGAknPEAAKAFIDWALSKEAQELLAkvGSY 260


                 ....*...
gi 488154076 300 LRPRNPEV 307
Cdd:cd13544  261 AIPTNPDA 268
YvgK COG1910
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];
139-171 8.17e-05

Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];


Pssm-ID: 441514 [Multi-domain]  Cd Length: 328  Bit Score: 43.84  E-value: 8.17e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 488154076 139 FLVRKNNPKQIRDWNDLAKDGVNIViaN-PKTSG 171
Cdd:COG1910  183 LIVAKGNPKGIKGLEDLARPDLRFV--NrQKGSG 214
PBP2_ModA_like cd00993
Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein ...
 74-292 5.63e-04

Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein fold; Molybdate binding domain ModA. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has revealed a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. This octahedral geometry was rather unexpected. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270215 [Multi-domain]  Cd Length: 225  Bit Score: 40.78  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  74 TSVSIQQSHGGSSKQALSVANGLQADVVTMNQSSDIDLLEKKGLVEKGWQQALpdhaapYTSTMVFLVRKNNPKQIRDWN 153
Cdd:cd00993   25 TGVTVVLNFGSSGALAKQIEQGAPADVFISADQKWMDYLVAAGLILPASVRPF------AGNRLVLVVPKASPVSGTPLL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076 154 DLAKD-GVNIVIANPKTSGNGRYAFLGAYGYGLKTTNGNeqeaqKLvasilkntpVFENGGRAATTTFTQRNIgDVLITf 232
Cdd:cd00993   99 ELALDeGGRIAVGDPQSVPAGRYAKQVLEKLGLWDKLPP-----KL---------VEAPDVRQVLGLVESGEA-DAGFV- 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488154076 233 eneanYVSKKLTQGQFEIVY---PSYTISAESPVAVVNSVVAKkgtqKTARAYLEYLWSEPAQ 292
Cdd:cd00993  163 -----YASDALAAKKVKVVAtlpEDLHEPIVYPVAVLKGSKNK----AEAKAFLDFLLSPEGQ 216
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 34-289 1.05e-03

PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 40.22  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   34 NTESDGKNITLLNASYDvarDFYKEYNPLFIKTYQSEHPGTSVSIqqSHGGSSKQALSVANGLqADVVtmnqSSDIDLLE 113
Cdd:pfam12849   1 SAAASAPTVGTILIAGS---STQAPGLLDLAEAFEKKYPGAKVKV--TSVGSGEGIKALLNGD-VDVA----LVSRPLTE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  114 KKgLVEKGWQQALPDHAAPY-TSTMVFLVRKNNPK--------------QIRDWNDLAKDGVNIVIANPKTSGNGRYAFL 178
Cdd:pfam12849  71 EE-FEAFGANGAGGLVEVPVaYDGIAIVVNKDNPAniltvealkkifsgKITNWNDGGPDGPIKFVSRGDNSGTTELFST 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076  179 GAYGYGLKTTNGNEQEAQKLVASILKNtpvfENGGRAATTTFTQRNIGDvLITFENEANYVSKKLTQGQFEIVYPSYTIS 258
Cdd:pfam12849 150 HLKEKGPWGAAGIGAAGSPGVASVVAG----PGAIGYVEVSYALANLGY-TLADVAGGTYLSFAKALKVAKINPGAGLVI 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 488154076  259 A--------ESPVAVVNSVVAKKGTQKT---ARAYLEYLWSE 289
Cdd:pfam12849 225 PleeaiadgDYPLSRPYYVIVKNPPKGPaplAKAFLDFLLSD 266
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
 139-163 3.54e-03

PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It is often associated with a helix-turn-helix domain.


Pssm-ID: 463683 [Multi-domain]  Cd Length: 192  Bit Score: 37.94  E-value: 3.54e-03
                          10        20
                  ....*....|....*....|....*
gi 488154076  139 FLVRKNNPKQIRDWNDLAKDGVNIV 163
Cdd:pfam12727  73 LVVAPGNPKGITGWEDLARPGLRFV 97
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
 88-301 3.76e-03

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 38.08  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076    88 QALSVANGLQADVVTMNQSSDIDLLeKKGLVEKGWQQALP--------DHAAPY-TSTMVFLVRKNNPkqIRDWNDLAkd 158
Cdd:smart00062  31 KAIAKELGLKVEFVEVSFDSLLTAL-KSGKIDVVAAGMTItperakqvDFSDPYyRSGQVILVRKDSP--IKSLEDLK-- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154076   159 gvNIVIANPKTSGNGRYAFLGAYGYGLKTTNGNEQEAQKLVAsilkntpvfengGRAatttftqrnigDVLITFENEANY 238
Cdd:smart00062 106 --GKKVAVVAGTTAEELLKKLYPEAKIVSYDSNAEALAALKA------------GRA-----------DAAVADAPLLAA 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488154076   239 VSKKLTQGQFEIVYPSYTISAESPVAVvnsvvaKKGTQKTARAYLEYLWSEPAQELAASLYLR 301
Cdd:smart00062 161 LVKQHGLPELKIVPDPLDTPEGYAIAV------RKGDPELLDKINKALKELKADGTLKKISEK 217
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH